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OS25_PLAGA
ID   OS25_PLAGA              Reviewed;         215 AA.
AC   P13401;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=25 kDa ookinete surface antigen;
DE   AltName: Full=Pgs25;
DE   Flags: Precursor;
OS   Plasmodium gallinaceum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX   NCBI_TaxID=5849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=2468086; DOI=10.1016/0166-6851(89)90090-x;
RA   Kaslow D.C., Syin C., McCutchan T.F., Miller L.H.;
RT   "Comparison of the primary structure of the 25 kDa ookinete surface
RT   antigens of Plasmodium falciparum and Plasmodium gallinaceum reveal six
RT   conserved regions.";
RL   Mol. Biochem. Parasitol. 33:283-287(1989).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-
CC       anchor {ECO:0000305}.
CC   -!- DEVELOPMENTAL STAGE: Expressed on zygotes and ookinetes.
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DR   EMBL; J04008; AAA29487.1; -; mRNA.
DR   AlphaFoldDB; P13401; -.
DR   SMR; P13401; -.
DR   VEuPathDB; PlasmoDB:PGAL8A_00490300; -.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0009986; C:cell surface; IEA:InterPro.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR010423; Pvs25/Psv28_EGF.
DR   Pfam; PF06247; Plasmod_Pvs28; 2.
DR   SMART; SM00181; EGF; 4.
DR   PROSITE; PS01186; EGF_2; 3.
PE   2: Evidence at transcript level;
KW   Cell membrane; Disulfide bond; EGF-like domain; Glycoprotein; GPI-anchor;
KW   Lipoprotein; Malaria; Membrane; Repeat; Signal.
FT   SIGNAL          1..16
FT   CHAIN           17..192
FT                   /note="25 kDa ookinete surface antigen"
FT                   /id="PRO_0000024569"
FT   PROPEP          193..215
FT                   /note="Removed in mature form"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000024570"
FT   DOMAIN          29..58
FT                   /note="EGF-like 1; truncated"
FT   DOMAIN          59..104
FT                   /note="EGF-like 2"
FT   DOMAIN          104..148
FT                   /note="EGF-like 3"
FT   DOMAIN          151..191
FT                   /note="EGF-like 4"
FT   LIPID           192
FT                   /note="GPI-anchor amidated serine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        144
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        163
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..78
FT                   /evidence="ECO:0000250"
FT   DISULFID        72..90
FT                   /evidence="ECO:0000250"
FT   DISULFID        92..103
FT                   /evidence="ECO:0000250"
FT   DISULFID        108..118
FT                   /evidence="ECO:0000250"
FT   DISULFID        113..131
FT                   /evidence="ECO:0000250"
FT   DISULFID        133..147
FT                   /evidence="ECO:0000250"
FT   DISULFID        155..166
FT                   /evidence="ECO:0000250"
FT   DISULFID        159..175
FT                   /evidence="ECO:0000250"
FT   DISULFID        177..190
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   215 AA;  24556 MW;  10FAEB06676D4DC9 CRC64;
     MNMSYLFFFF FIQLVLKYIN SKVTENTICK DGFLIQMSNH FECNCNPGFV LTSESTCENK
     VECNANSLDK RCGDFSKCAY KDLQQKELTC KCIDGYDLEE SICVPNECKN FRCESGKCVL
     DPKQEAKIPM CSCFIGIVPS KENNNTCTIE GQTECTLKCT KENETCKKTS GIYKCDCKDG
     YTFDKEENAC ISFSLFNILN LSIIFIISLI YFYII
 
 
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